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Sensor protein PhoQ (EC 2.7.13.3) (EC 3.1.3.-) (Sensor histidine protein kinase/phosphatase PhoQ)

 PHOQ_ECOLI              Reviewed;         486 AA.
P23837;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
25-OCT-2017, entry version 176.
RecName: Full=Sensor protein PhoQ;
EC=2.7.13.3;
EC=3.1.3.-;
AltName: Full=Sensor histidine protein kinase/phosphatase PhoQ;
Name=phoQ; OrderedLocusNames=b1129, JW1115;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1729240; DOI=10.1128/jb.174.2.492-498.1992;
Kasahara M., Nakata A., Shinagawa H.;
"Molecular analysis of the Escherichia coli phoP-phoQ operon.";
J. Bacteriol. 174:492-498(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
STRAIN=K12;
PubMed=1530848; DOI=10.1128/jb.174.2.486-491.1992;
Groisman E.A., Heffron F., Solomon F.;
"Molecular genetic analysis of the Escherichia coli phoP locus.";
J. Bacteriol. 174:486-491(1992).
[6]
PROTEIN SEQUENCE OF 43-190, SECONDARY STRUCTURE OF SENSOR DOMAIN, AND
MUTAGENESIS OF 148-GLU--GLU-154.
STRAIN=BL21-DE3, and K12 / CSH26;
PubMed=8900137; DOI=10.1074/jbc.271.43.26630;
Waldburger C.D., Sauer R.T.;
"Signal detection by the PhoQ sensor-transmitter. Characterization of
the sensor domain and a response-impaired mutant that identifies
ligand-binding determinants.";
J. Biol. Chem. 271:26630-26636(1996).
[7]
FUNCTION, AND INDUCTION BY LOW MG(2+).
STRAIN=K12 / MC4100 / JA176;
PubMed=10464230;
Kato A., Tanabe H., Utsumi R.;
"Molecular characterization of the PhoP-PhoQ two-component system in
Escherichia coli K-12: identification of extracellular Mg2+-responsive
promoters.";
J. Bacteriol. 181:5516-5520(1999).
[8]
MUTAGENESIS OF SENSOR PERIPLASMIC DOMAIN, AND MUTAGENESIS OF THR-48.
STRAIN=K12 / CSH26;
PubMed=12218035; DOI=10.1128/JB.184.19.5468-5478.2002;
Regelmann A.G., Lesley J.A., Mott C., Stokes L., Waldburger C.D.;
"Mutational analysis of the Escherichia coli PhoQ sensor kinase:
differences with the Salmonella enterica serovar Typhimurium PhoQ
protein and in the mechanism of Mg2+ and Ca2+ sensing.";
J. Bacteriol. 184:5468-5478(2002).
[9]
ENZYME REGULATION, AND KINETIC PARAMETERS.
STRAIN=K12 / CSH26;
PubMed=12670981; DOI=10.1128/JB.185.8.2563-2570.2003;
Lesley J.A., Waldburger C.D.;
"Repression of Escherichia coli PhoP-PhoQ signaling by acetate reveals
a regulatory role for acetyl coenzyme A.";
J. Bacteriol. 185:2563-2570(2003).
[10]
GENOME-WIDE ANALYSIS, AND REGULATION BY MG(2+).
STRAIN=K12 / MC4100 / JA176;
PubMed=12813061; DOI=10.1128/JB.185.13.3696-3702.2003;
Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
Mori H., Ishihama A., Utsumi R.;
"Identification and molecular characterization of the Mg2+ stimulon of
Escherichia coli.";
J. Bacteriol. 185:3696-3702(2003).
[11]
GENOME-WIDE ANALYSIS.
STRAIN=K12 / ST001;
PubMed=13129944; DOI=10.1128/JB.185.19.5735-5746.2003;
Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
Mizuno T.;
"Genome-wide analyses revealing a signaling network of the RcsC-YojN-
RcsB phosphorelay system in Escherichia coli.";
J. Bacteriol. 185:5735-5746(2003).
[12]
INTERACTION WITH EVGA/EVGS.
STRAIN=K12 / MC4100 / JA176;
PubMed=15126461; DOI=10.1128/JB.186.10.3006-3014.2004;
Eguchi Y., Okada T., Minagawa S., Oshima T., Mori H., Yamamoto K.,
Ishihama A., Utsumi R.;
"Signal transduction cascade between EvgA/EvgS and PhoP/PhoQ two-
component systems of Escherichia coli.";
J. Bacteriol. 186:3006-3014(2004).
[13]
MUTAGENESIS OF THR-47; ASN-68; ASP-90; ASP-149; ASP-150; ASP-151;
ASP-152 AND ASP-179.
STRAIN=BL21-DE3, and K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=16041131; DOI=10.1271/bbb.69.1281;
Minagawa S., Okura R., Tsuchitani H., Hirao K., Yamamoto K.,
Utsumi R.;
"Isolation and molecular characterization of the locked-on mutant of
Mg(2+) sensor PhoQ in Escherichia coli.";
Biosci. Biotechnol. Biochem. 69:1281-1287(2005).
[14]
REGULATION OF ACID RESISTANCE GENES.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15703297; DOI=10.1073/pnas.0408238102;
Zwir I., Shin D., Kato A., Nishino K., Latifi T., Solomon F.,
Hare J.M., Huang H., Groisman E.A.;
"Dissecting the PhoP regulatory network of Escherichia coli and
Salmonella enterica.";
Proc. Natl. Acad. Sci. U.S.A. 102:2862-2867(2005).
[15]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[16]
ENZYME REGULATION, AND PROBABLE INTERACTION WITH MGRB.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=20041203; DOI=10.1371/journal.pgen.1000788;
Lippa A.M., Goulian M.;
"Feedback inhibition in the PhoQ/PhoP signaling system by a membrane
peptide.";
PLoS Genet. 5:E1000788-E1000788(2009).
[17]
ENZYME REGULATION, AND INDUCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22267510; DOI=10.1128/JB.06055-11;
Lippa A.M., Goulian M.;
"Perturbation of the oxidizing environment of the periplasm stimulates
the PhoQ/PhoP system in Escherichia coli.";
J. Bacteriol. 194:1457-1463(2012).
[18]
MUTAGENESIS OF VAL-27; LEU-30; LEU-199; ASN-202; LEU-203 AND LEU-205,
AND ROLE OF ASN-202 IN SIGNALING.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=20404199; DOI=10.1073/pnas.1003166107;
Goldberg S.D., Clinthorne G.D., Goulian M., DeGrado W.F.;
"Transmembrane polar interactions are required for signaling in the
Escherichia coli sensor kinase PhoQ.";
Proc. Natl. Acad. Sci. U.S.A. 107:8141-8146(2010).
[19]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 335-486 IN COMPLEX WITH ATP
ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, MG(2+)-BINDING, AND MUTAGENESIS
OF LYS-392; ARG-434 AND ARG-439.
STRAIN=BL21;
PubMed=11493605; DOI=10.1074/jbc.M106080200;
Marina A., Mott C., Auyzenberg A., Hendrickson W.A., Waldburger C.D.;
"Structural and mutational analysis of the PhoQ histidine kinase
catalytic domain. Insight into the reaction mechanism.";
J. Biol. Chem. 276:41182-41190(2001).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-190 OF WILD-TYPE IN
COMPLEX WITH NICKEL IONS AND MUTANT
148-GLN-ASN-ASN-ASN-ASN-ALA-GLN-154, SUBUNIT, PERIPLASMIC SENSOR
DOMAIN, AND MUTAGENESIS OF ARG-50; GLY-54 AND ASP-179.
STRAIN=K12 / CSH26;
PubMed=18348979; DOI=10.1074/jbc.M710592200;
Cheung J., Bingman C.A., Reyngold M., Hendrickson W.A.,
Waldburger C.D.;
"Crystal structure of a functional dimer of the PhoQ sensor domain.";
J. Biol. Chem. 283:13762-13770(2008).
-!- FUNCTION: Member of the two-component regulatory system PhoP/PhoQ
involved in adaptation to low Mg(2+) environments and the control
of acid resistance genes. In low periplasmic Mg(2+), PhoQ
functions as a membrane-associated protein kinase that undergoes
autophosphorylation and subsequently transfers the phosphate to
PhoP, resulting in the expression of PhoP-activated genes (PAG)
and repression of PhoP-repressed genes (PRG). In high periplasmic
Mg(2+), acts as a protein phosphatase that dephosphorylates
phospho-PhoP, resulting in the repression of PAG and may lead to
expression of some PRG (By similarity). PhoP-regulated
transcription is redox-sensitive, being activated when the
periplasm becomes more reducing (deletion of dsbA/dsbB, or
treatment with dithiothreitol). MgrB acts between DsbA/DsbB and
PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB
are required for its action on PhoQ, which then acts on PhoP.
Mediates magnesium influx to the cytosol by activation of mgtA.
Promotes expression of the two-component regulatory system
rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR
and yrbL genes. {ECO:0000250, ECO:0000269|PubMed:10464230}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine.
-!- ENZYME REGULATION: Acetyl-CoA acts as a non-competitive inhibitor
of the PhoQ autokinase activity. Feedback inhibited by MgrB, which
seems to bind PhoQ, altering its activity and that of downstream
effector PhoP. {ECO:0000269|PubMed:12670981,
ECO:0000269|PubMed:20041203, ECO:0000269|PubMed:22267510}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20.93 uM for ATP (at 22 degrees Celsius and pH 8, in the
presence of 50 mM KCl and 1 mM MgCl(2))
{ECO:0000269|PubMed:11493605, ECO:0000269|PubMed:12670981};
KM=55 uM for ATP (at 22 degrees Celsius and pH 8, in the
presence of 25 mM KCl and 0.4 mM MgCl(2))
{ECO:0000269|PubMed:11493605, ECO:0000269|PubMed:12670981};
-!- SUBUNIT: Homodimer; probably dimerizes via the cytoplasmic domain
(Probable). Probably interacts with MgrB in the periplasm,
altering its activity and that of downstream effector PhoP.
{ECO:0000269|PubMed:11493605, ECO:0000269|PubMed:15126461,
ECO:0000269|PubMed:18348979, ECO:0000305}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1113605, EBI-1113605;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
{ECO:0000269|PubMed:15919996}.
-!- INDUCTION: The phoP/phoQ operon is positively autoregulated by
both PhoP and PhoQ in a Mg(2+)-dependent manner, inhibited at high
Mg(2+) concentrations (PubMed:10464230). Induced by dsbA
disruption and dithiothreitol (PubMed:22267510).
{ECO:0000269|PubMed:10464230, ECO:0000269|PubMed:22267510}.
-!- MISCELLANEOUS: There is a close linkage between the PhoP/PhoQ and
Rcs signaling systems, and both signaling systems respond to
certain external divalent cations (zinc and magnesium).
-!- MISCELLANEOUS: Two-component regulatory system EvgA/EvgS interacts
with PhoP/PhoQ via signal transduction mediated by phospho-EvgA.
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EMBL; D90393; BAA14391.1; -; Genomic_DNA.
EMBL; U00096; AAC74213.1; -; Genomic_DNA.
EMBL; AP009048; BAA35951.1; -; Genomic_DNA.
EMBL; M81433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; B41966; B41966.
RefSeq; NP_415647.1; NC_000913.3.
RefSeq; WP_000735412.1; NZ_LN832404.1.
PDB; 1ID0; X-ray; 1.60 A; A=335-486.
PDB; 3BQ8; X-ray; 2.50 A; A/B=43-190.
PDB; 3BQA; X-ray; 2.00 A; A/B=43-190.
PDBsum; 1ID0; -.
PDBsum; 3BQ8; -.
PDBsum; 3BQA; -.
ProteinModelPortal; P23837; -.
SMR; P23837; -.
DIP; DIP-10501N; -.
IntAct; P23837; 2.
STRING; 316385.ECDH10B_1201; -.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
iPTMnet; P23837; -.
PaxDb; P23837; -.
PRIDE; P23837; -.
EnsemblBacteria; AAC74213; AAC74213; b1129.
EnsemblBacteria; BAA35951; BAA35951; BAA35951.
GeneID; 946326; -.
KEGG; ecj:JW1115; -.
KEGG; eco:b1129; -.
PATRIC; fig|1411691.4.peg.1137; -.
EchoBASE; EB0725; -.
EcoGene; EG10732; phoQ.
eggNOG; ENOG4105IFJ; Bacteria.
eggNOG; COG0642; LUCA.
HOGENOM; HOG000274481; -.
InParanoid; P23837; -.
KO; K07637; -.
PhylomeDB; P23837; -.
BioCyc; EcoCyc:PHOQ-MONOMER; -.
BRENDA; 2.7.13.3; 2026.
EvolutionaryTrace; P23837; -.
PRO; PR:P23837; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IMP:EcoCyc.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IMP:EcoCyc.
GO; GO:0010350; P:cellular response to magnesium starvation; IMP:EcoCyc.
GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR003660; HAMP_dom.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR015014; PhoQ_Sensor.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF08918; PhoQ_Sensor; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS50885; HAMP; 1.
PROSITE; PS50109; HIS_KIN; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Direct protein sequencing; Hydrolase; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Protein phosphatase; Reference proteome; Transferase;
Transmembrane; Transmembrane helix; Two-component regulatory system.
CHAIN 1 486 Sensor protein PhoQ.
/FTId=PRO_0000074837.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 194 Periplasmic. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TOPO_DOM 216 486 Cytoplasmic. {ECO:0000255}.
DOMAIN 215 266 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 274 480 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
NP_BIND 385 393 ATP.
NP_BIND 415 420 ATP.
NP_BIND 434 446 ATP.
METAL 151 151 Divalent metal cation.
METAL 152 152 Divalent metal cation.
METAL 385 385 Magnesium.
METAL 442 442 Magnesium.
SITE 202 202 Plays a critical role in the switching
between kinase and phosphatase states.
MOD_RES 277 277 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107}.
MUTAGEN 27 27 V->N: Shows Mg(2+)-dependent signaling
and partial gene activation activity;
when associated with A-202.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 30 30 L->N: Shows Mg(2+)-dependent signaling
and displays higher gene activation
activity than wild-type; when associated
with A-202.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 47 47 T->L: No significant effect (with or
without MgCl(2) or CaCl(2)).
{ECO:0000269|PubMed:16041131}.
MUTAGEN 48 48 T->A,C,E,M,N,Q,S,V: No significant effect
(with or without MgCl(2) or CaCl(2)).
{ECO:0000269|PubMed:12218035}.
MUTAGEN 48 48 T->D,G,H,I,K,L,P,R: Confers less than 30%
of the wild-type levels of PhoP/PhoQ-
signaling cascade in absence of CaCl(2)
or MgCl(2).
{ECO:0000269|PubMed:12218035}.
MUTAGEN 48 48 T->F,W: Decreased sensitivity to
repression by calcium but not by
magnesium. {ECO:0000269|PubMed:12218035}.
MUTAGEN 48 48 T->Y: Higher activity than wild-type
(with or without MgCl(2) or CaCl(2)).
{ECO:0000269|PubMed:12218035}.
MUTAGEN 50 50 R->D: Large decrease in the
transcriptional activation of PhoQ-
dependent genes.
{ECO:0000269|PubMed:18348979}.
MUTAGEN 54 54 G->D: Very large decrease in the
transcriptional activation of PhoQ-
dependent genes.
{ECO:0000269|PubMed:18348979}.
MUTAGEN 68 68 N->L: No significant effect (with or
without MgCl(2) or CaCl(2)).
{ECO:0000269|PubMed:16041131}.
MUTAGEN 90 90 D->A: No significant effect (with or
without MgCl(2) or CaCl(2)).
{ECO:0000269|PubMed:16041131}.
MUTAGEN 148 154 EDDDDAE->QNNNNAQ: Unable to bind divalent
cations in vitro and impaired in the
ability to respond to Mg(2+) deprivation
in vivo. {ECO:0000269|PubMed:8900137}.
MUTAGEN 149 149 D->A: Wild-type effect concerning mgrB
transcription.
{ECO:0000269|PubMed:16041131}.
MUTAGEN 150 150 D->I: Wild-type effect concerning mgrB
transcription.
{ECO:0000269|PubMed:16041131}.
MUTAGEN 151 151 D->I: Wild-type effect concerning mgrB
transcription.
{ECO:0000269|PubMed:16041131}.
MUTAGEN 152 152 D->F: Wild-type effect concerning mgrB
transcription.
{ECO:0000269|PubMed:16041131}.
MUTAGEN 179 179 D->L,A: Locked-on mutant defective in
Mg(2+)-sensing and unable to control its
phosphorylation state and phosphotransfer
to phoP. {ECO:0000269|PubMed:16041131,
ECO:0000269|PubMed:18348979}.
MUTAGEN 179 179 D->R: Very large decrease in the
transcriptional activation of PhoQ-
dependent genes.
{ECO:0000269|PubMed:16041131,
ECO:0000269|PubMed:18348979}.
MUTAGEN 199 199 L->N: Shows Mg(2+)-dependent signaling
and partial gene activation activity;
when associated with A-202.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 202 202 N->A: Is blind to signal, fails to
activate transcription of PhoQ-dependent
genes, and abrogates transcription when
coexpressed with wild-type PhoQ. Shows no
detectable autophosphorylation. Still
displays phosphatase activity. Recovers
Mg(2+)-dependent signaling and partial
gene activation activity; when associated
with N-27 or N-199 or N-203 or N-205.
Recovers Mg(2+)-dependent signaling and
displays higher gene activation activity
than wild-type; when associated with N-
30. {ECO:0000269|PubMed:20404199}.
MUTAGEN 202 202 N->I,L,M,F,W,Y,V,C,G,P: Is blind to
signal, fails to activate transcription
of PhoQ-dependent genes, and abrogates
transcription when coexpressed with wild-
type PhoQ. {ECO:0000269|PubMed:20404199}.
MUTAGEN 202 202 N->R,D,Q,E,H: Shows similar activity
profile to wild-type.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 203 203 L->N: Shows Mg(2+)-dependent signaling
and partial gene activation activity;
when associated with A-202.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 205 205 L->N: Shows Mg(2+)-dependent signaling
and partial gene activation activity;
when associated with A-202.
{ECO:0000269|PubMed:20404199}.
MUTAGEN 392 392 K->A: 44-fold decrease in ATP affinity
and 6-fold decrease in activity.
{ECO:0000269|PubMed:11493605}.
MUTAGEN 434 434 R->A: 2-fold decrease in ATP affinity and
51-fold decrease in activity.
{ECO:0000269|PubMed:11493605}.
MUTAGEN 439 439 R->A: 3-fold decrease in ATP affinity and
2-fold increase in activity.
{ECO:0000269|PubMed:11493605}.
HELIX 46 62 {ECO:0000244|PDB:3BQA}.
STRAND 64 66 {ECO:0000244|PDB:3BQA}.
STRAND 69 71 {ECO:0000244|PDB:3BQA}.
HELIX 76 79 {ECO:0000244|PDB:3BQA}.
STRAND 85 89 {ECO:0000244|PDB:3BQA}.
STRAND 95 100 {ECO:0000244|PDB:3BQA}.
HELIX 103 108 {ECO:0000244|PDB:3BQA}.
HELIX 111 113 {ECO:0000244|PDB:3BQA}.
STRAND 114 116 {ECO:0000244|PDB:3BQA}.
STRAND 118 125 {ECO:0000244|PDB:3BQA}.
HELIX 126 133 {ECO:0000244|PDB:3BQA}.
HELIX 137 148 {ECO:0000244|PDB:3BQA}.
STRAND 154 164 {ECO:0000244|PDB:3BQA}.
STRAND 168 170 {ECO:0000244|PDB:3BQA}.
STRAND 173 178 {ECO:0000244|PDB:3BQA}.
HELIX 183 185 {ECO:0000244|PDB:3BQA}.
STRAND 337 339 {ECO:0000244|PDB:1ID0}.
HELIX 340 354 {ECO:0000244|PDB:1ID0}.
TURN 355 358 {ECO:0000244|PDB:1ID0}.
STRAND 361 365 {ECO:0000244|PDB:1ID0}.
STRAND 371 374 {ECO:0000244|PDB:1ID0}.
HELIX 376 393 {ECO:0000244|PDB:1ID0}.
STRAND 395 404 {ECO:0000244|PDB:1ID0}.
STRAND 409 418 {ECO:0000244|PDB:1ID0}.
HELIX 422 424 {ECO:0000244|PDB:1ID0}.
HELIX 427 429 {ECO:0000244|PDB:1ID0}.
HELIX 446 455 {ECO:0000244|PDB:1ID0}.
STRAND 459 464 {ECO:0000244|PDB:1ID0}.
STRAND 468 476 {ECO:0000244|PDB:1ID0}.
SEQUENCE 486 AA; 55300 MW; 89C6D97A3C9B8809 CRC64;
MKKLLRLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY
TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR DVPWLMKMIQ PDWLKSNGFH
EIEADVNDTS LLLSGDHSIQ QQLQEVREDD DDAEMTHSVA VNVYPATSRM PKLTIVVVDT
IPVELKSSYM VWSWFIYVLS ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN
PATTRELTSL VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV
SDAEPVMLEQ ISRISQQIGY YLHRASMRGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV
NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI
PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITEQYEGKI VAGESMLGGA RMEVIFGRQH
SAPKDE


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